Authors: K.S. Jin, S. Jin, J. Yoon, K. Heo, J. Kim and M. Ree
Affilation: Pohang University of Science and Technology, Korea
Pages: 646 - 647
Keywords: porcine pepsin, solution SAXS
To understand the conformational behavior of a protein, it is necessary to define not only the structure of its native state but also that of various denatured states. Recent studies have revealed the biological significance of denatured states in processes such as aggregation, chaperone binding, and transport across membrane. A variety of denatured states have also been identified, differing in their overall dimensions and the extent of residual secondary and tertiary structures. Pepsin is a particularly good model for the study of conformational behavior under several conditions because detailed information is available on its secondary structure, enzymatic properties, and zymogen activation. Solution small angle X-ray scattering (SAXS) is an effective technique for measuring structure and structural difference of protein under various environments. In this study, the structural characteristics of various conformational states of porcine pepsin were studied in terms of size and shape under several pH conditions by solution SAXS.
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